Recombinant Mouse Acetylcholinesterase/ACHE Protein (His Tag)

Specifications

Catalog number

PKSM040622

Size / count

20 µg

Dry ice

No

Hazardous

No

Discontinued

No

Background

Acetylcholinesterase, also known as ACHE, is an enzyme that degrades the neurotransmitter acetylcholine, producing choline and an acetate group. ACHE plays a crucial role in nerve impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter acetylcholine (ACh) . ACHE appears to be a potential therapeutic target at muscle injuries including organophosphate myopathy. It is an externally oriented membrane-bound enzyme and its main physiological role is termination of chemical transmission at cholinergic synapses and secretory organs by rapid hydrolysis of the neurotransmitter acetylcholine (ACh) . ACHE plays important roles in the cholinergic system, and its dysregulation is involved in a variety of human diseases. ACHE was significantly down-regulated in the cancerous tissues of 69.2% of hepatocellular carcinoma (HCC) patients, and the low ACHE expression in HCC was correlated with tumor aggressiveness, an elevated risk of postoperative recurrence, and a low survival rate. Both the recombinant ACHE protein and the enhanced expression of ACHE significantly inhibited HCC cell growth in vitro and tumorigenicity in vivo. ACHE as a tumor growth suppressor in regulating cell proliferation, the relevant signaling pathways, and the drug sensitivity of HCC cells. Thus, ACHE is a promising independent prognostic predictor for HCC recurrence and the survival of HCC patients. ACHE is inhibited by organophosphate and carbamate pesticides. However, this enzyme is only slightly inhibited by organophosphorothionates.

Synonyms

ME1a; mE1b; mE1c; mE1c-long; mE1d; mE1d'; mE1e

UniProt

P21836

Accession Number

NP_033729.1

Expression System

HEK293 Cells

Tag

C-His

Sequence

Met 1-Leu 614

Applications

Enzyme

Endotoxin

< 1.0 EU per μg of the protein as determined by the LAL method.

Purity

> 97 % as determined by reducing SDS-PAGE.

Bioactivity

Measured by its ability to cleave Acetylthiocholine. The specific activity is > 250 nmols/min/μg.

Reconstitution

Please refer to the printed manual for detailed information.

Shipping Conditions

This product is provided as lyophilized powder which is shipped with ice packs.

Storage Conditions

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Calculated Molecular Weight

66.2 kDa

Observed Molecular Weight

66.2 kDa

Species

Mouse